AT8B1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AT8B1_HUMAN
• UniProt AC: O43520
• Protein Name: Phospholipid-transporting ATPase IC
• Gene Name: ATP8B1
• Organism: Homo sapiens (Human).
• Sequence Length: 1251
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein. Apical cell membrane . Cell projection, stereocilium . Endoplasmic reticulum . Golgi apparatus . Exit from the endoplasmic reticulum requires the presence of TMEM30A or TMEM30B (PubMed:20947505). Localizes
• Protein Description: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. May play a role in asymmetric distribution of phospholipids in the canicular membrane. May have a role in transport of bile acids into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both. In cooperation with ABCB4 may be involved in establishing integrity of the canalicular membrane thus protecting hepatocytes from bile salts. Together with TMEM30A is involved in uptake of the synthetic drug alkylphospholipid perifosine. Involved in the microvillus formation in polarized epithelial cells; the function seems to be independent from its flippase activity. Required for the preservation of cochlear hair cells in the inner ear. May act as cardiolipin transporter during inflammatory injury..
• Protein Sequence: MSTERDSETTFDEDSQPNDEVVPYSDDETEDELDDQGSAVEPEQNRVNREAEENREPFRKECTWQVKANDRKYHEQPHFMNTKFLCIKESKYANNAIKTYKYNAFTFIPMNLFEQFKRAANLYFLALLILQAVPQISTLAWYTTLVPLLVVLGVTAIKDLVDDVARHKMDKEINNRTCEVIKDGRFKVAKWKEIQVGDVIRLKKNDFVPADILLLSSSEPNSLCYVETAELDGETNLKFKMSLEITDQYLQREDTLATFDGFIECEEPNNRLDKFTGTLFWRNTSFPLDADKILLRGCVIRNTDFCHGLVIFAGADTKIMKNSGKTRFKRTKIDYLMNYMVYTIFVVLILLSAGLAIGHAYWEAQVGNSSWYLYDGEDDTPSYRGFLIFWGYIIVLNTMVPISLYVSVEVIRLGQSHFINWDLQMYYAEKDTPAKARTTTLNEQLGQIHYIFSDKTGTLTQNIMTFKKCCINGQIYGDHRDASQHNHNKIEQVDFSWNTYADGKLAFYDHYLIEQIQSGKEPEVRQFFFLLAVCHTVMVDRTDGQLNYQAASPDEGALVNAARNFGFAFLARTQNTITISELGTERTYNVLAILDFNSDRKRMSIIVRTPEGNIKLYCKGADTVIYERLHRMNPTKQETQDALDIFANETLRTLCLCYKEIEEKEFTEWNKKFMAASVASTNRDEALDKVYEEIEKDLILLGATAIEDKLQDGVPETISKLAKADIKIWVLTGDKKETAENIGFACELLTEDTTICYGEDINSLLHARMENQRNRGGVYAKFAPPVQESFFPPGGNRALIITGSWLNEILLEKKTKRNKILKLKFPRTEEERRMRTQSKRRLEAKKEQRQKNFVDLACECSAVICCRVTPKQKAMVVDLVKRYKKAITLAIGDGANDVNMIKTAHIGVGISGQEGMQAVMSSDYSFAQFRYLQRLLLVHGRWSYIRMCKFLRYFFYKNFAFTLVHFWYSFFNGYSAQTAYEDWFITLYNVLYTSLPVLLMGLLDQDVSDKLSLRFPGLYIVGQRDLLFNYKRFFVSLLHGVLTSMILFFIPLGAYLQTVGQDGEAPSDYQSFAVTIASALVITVNFQIGLDTSYWTFVNAFSIFGSIALYFGIMFDFHSAGIHVLFPSAFQFTGTASNALRQPYIWLTIILAVAVCLLPVVAIRFLSMTIWPSESDKIQKHRKRLKAEEQWQRRQQVFRRGVSTRRSAYAFSHQRGYADLISSGRSIRKKRSPLDAIVADGTAEYRRTGDS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	ETTFDEDSQPNDEVV CCCCCCCCCCCCCCC	45.55	28348404
24	Phosphorylation	PNDEVVPYSDDETED CCCCCCCCCCCCCCC	17.08	28348404
25	Phosphorylation	NDEVVPYSDDETEDE CCCCCCCCCCCCCCC	32.30	29802988
29	Phosphorylation	VPYSDDETEDELDDQ CCCCCCCCCCCCCCC	56.59	29802988
38	Phosphorylation	DELDDQGSAVEPEQN CCCCCCCCCCCHHHH	24.41	28348404
60	Methylation	ENREPFRKECTWQVK HHCCCCHHHCCEEEE	58.48	23644510
417	Ubiquitination	VIRLGQSHFINWDLQ EEECCCCEEECCEEE	21.51	22817900
438	Phosphorylation	DTPAKARTTTLNEQL CCCCCCCCCCHHHHH	29.06	29759185
439	Phosphorylation	TPAKARTTTLNEQLG CCCCCCCCCHHHHHC	24.59	29759185
440	Phosphorylation	PAKARTTTLNEQLGQ CCCCCCCCHHHHHCC	27.29	29759185
455	Ubiquitination	IHYIFSDKTGTLTQN EEEEEECCCCCEECC	47.89	22817900
476	Phosphorylation	CCINGQIYGDHRDAS HEECCEECCCCCCCH	14.49	-
584	Phosphorylation	ITISELGTERTYNVL EEEECCCCCCEEEEE	34.61	24719451
609	Phosphorylation	RMSIIVRTPEGNIKL EEEEEEECCCCCEEE	18.13	29396449
615	Methylation	RTPEGNIKLYCKGAD ECCCCCEEEEECCCC	37.09	-
639	Ubiquitination	MNPTKQETQDALDIF CCCCCCHHHHHHHHH	29.29	29901268
658	Phosphorylation	LRTLCLCYKEIEEKE HHHHHHHHHHHHHHH	9.94	-
667	Phosphorylation	EIEEKEFTEWNKKFM HHHHHHCHHHHHHHH	40.98	24719451
689	Ubiquitination	NRDEALDKVYEEIEK CHHHHHHHHHHHHHH	47.79	29901268
779	Phosphorylation	QRNRGGVYAKFAPPV CCCCCCCCCCCCCCC	13.83	-
789	Phosphorylation	FAPPVQESFFPPGGN CCCCCCCCCCCCCCC	18.33	-
902	Acetylation	ANDVNMIKTAHIGVG CCCCCEEEEEEEECC	28.96	19825509
924	Phosphorylation	QAVMSSDYSFAQFRY HHHHCCCCCHHHHHH	13.98	-
925	Phosphorylation	AVMSSDYSFAQFRYL HHHCCCCCHHHHHHH	21.06	-
931	Phosphorylation	YSFAQFRYLQRLLLV CCHHHHHHHHHHHHH	14.42	26074081
992	Phosphorylation	ITLYNVLYTSLPVLL HHHHHHHHHHHHHHH	7.04	-
1012	Phosphorylation	QDVSDKLSLRFPGLY CCCCHHHCCCCCCEE	24.20	24719451
1173	Phosphorylation	LSMTIWPSESDKIQK HHCCCCCCCHHHHHH	34.43	29759185
1175	Phosphorylation	MTIWPSESDKIQKHR CCCCCCCHHHHHHHH	48.84	29759185
1203	Phosphorylation	QVFRRGVSTRRSAYA HHHHHCCCHHHHHHH	21.01	24719451
1204	Phosphorylation	VFRRGVSTRRSAYAF HHHHCCCHHHHHHHH	27.91	-
1207	Phosphorylation	RGVSTRRSAYAFSHQ HCCCHHHHHHHHCCC	23.49	25849741
1209	Phosphorylation	VSTRRSAYAFSHQRG CCHHHHHHHHCCCCC	14.93	23911959
1212	Phosphorylation	RRSAYAFSHQRGYAD HHHHHHHCCCCCHHH	15.56	29038488
1217	Phosphorylation	AFSHQRGYADLISSG HHCCCCCHHHHHHCC	10.11	27273156
1222	Phosphorylation	RGYADLISSGRSIRK CCHHHHHHCCCCCCC	33.75	25849741
1223	Phosphorylation	GYADLISSGRSIRKK CHHHHHHCCCCCCCC	31.09	26356563
1226	Phosphorylation	DLISSGRSIRKKRSP HHHHCCCCCCCCCCC	30.21	23312004
1232	Phosphorylation	RSIRKKRSPLDAIVA CCCCCCCCCCHHEEE	38.40	23312004
1242	Phosphorylation	DAIVADGTAEYRRTG HHEEECCCHHHHCCC	19.50	-
1245	Phosphorylation	VADGTAEYRRTGDS- EECCCHHHHCCCCC-	11.70	27259358

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of AT8B1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AT8B1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of AT8B1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CC50A_HUMAN	TMEM30A	physical	21914794
CC50B_HUMAN	TMEM30B	physical	21914794

Drug and Disease Associations

• Kegg Disease
• H00624: Familial cholestasis, including: Progressive familial intrahepatic cholestasis (PFIC); Benign recurr
• OMIM Disease
• 211600: Cholestasis, progressive familial intrahepatic, 1 (PFIC1)
• 243300: Cholestasis, benign recurrent intrahepatic, 1 (BRIC1)
• 147480: Cholestasis of pregnancy, intrahepatic 1 (ICP1)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1217, AND MASSSPECTROMETRY.
PubMed: 19534553